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Titolo:
STRUCTURAL AND IMMUNOLOGICAL STUDIES OF GPI-ANCHORED BRUSH-BORDER HYDROLASES
Autore:
TURNER AJ;
Indirizzi:
UNIV LEEDS,DEPT BIOCHEM & MOLEC BIOL LEEDS LS2 9JT ENGLAND
Titolo Testata:
Brazilian journal of medical and biological research
fascicolo: 2, volume: 27, anno: 1994,
pagine: 389 - 394
SICI:
0100-879X(1994)27:2<389:SAISOG>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALKALINE-PHOSPHATASE; RENAL DIPEPTIDASE; MEMBRANE-PROTEINS; MOLECULAR-CLONING; CDNA CLONING; PHOSPHATIDYLINOSITOL; PURIFICATION; AMINOPEPTIDASE; EXPRESSION; ECTOENZYME;
Keywords:
GPI ANCHORS; PHOSPHOLIPASES; MEMBRANE DIPEPTIDASE; AMINOPEPTIDASE P;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
18
Recensione:
Indirizzi per estratti:
Citazione:
A.J. Turner, "STRUCTURAL AND IMMUNOLOGICAL STUDIES OF GPI-ANCHORED BRUSH-BORDER HYDROLASES", Brazilian journal of medical and biological research, 27(2), 1994, pp. 389-394

Abstract

The complement of brush border hydrolases provides an excellent modelsystem for study of the structure, topology and assembly of plasma membrane proteins. Among the peptidases of the renal brush border are a number of glycosylphosphatidylinositol (GPI)-anchored proteins, especially membrane dipeptidase and aminopeptidase P. Affinity purification protocols have led to the isolation of homogeneous forms of these proteins and membrane dipeptidase has been cloned and expressed in Xenopusoocytes and Cos-1 cells. The core glycan structures of both human andporcine dipeptidase have beeh determined, allowing direct comparisonsof the GPI anchors on the same protein in different species. Aminopeptidase P has been compared in the brush borders of pig kidney and intestine and may well be anchored in distinct ways in the two tissues. Immunological cross-reactivity of polyclonal antibodies to these two proteins has revealed the phospholipase C-cleaved GPI anchor as the common epitope and defined those components of the anchor important for recognition. These antibodies are also proving useful in characterizing GPI-derived mediators that may be involved in cell signalling processes. These abundant ectopeptidases offer a number of advantages for studies of the biochemistry of mammalian GPI anchors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 06:36:24